Related Experiment Video
Updated: Mar 11, 2026

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
Published on: September 28, 2018
Regulation of receptor-type protein tyrosine phosphatases by their C-terminal tail domains
Maayan Barnea1, Tsviya Olender1, Mark T Bedford2
1Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel.
Abstract:
Protein tyrosine phosphatases (PTPs) perform specific functions in vivo, despite being vastly outnumbered by their substrates. Because of this and due to the central roles PTPs play in regulating cellular function, PTP activity is regulated by a large variety of molecular mechanisms. We review evidence that indicates that the divergent C-terminal tail sequences (C-terminal domains, CTDs) of receptor-type PTPs (RPTPs) help regulate RPTP function by controlling intermolecular associations in a way that is itself subject to physiological regulation. We propose that the CTD of each RPTP defines an 'interaction code' that helps determine molecules it will interact with under various physiological conditions, thus helping to regulate and diversify PTP function.
Related Concept Videos
Receptor Tyrosine Kinases
Amplifying Signals via Enzymatic Cascade
Tail-anchoring of Proteins in the ER Membrane
Receptor Downregulation in MVBs
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....

